Low-specificity L-threonine aldolase

Low-specificity L-threonine aldolase
Identifiers
EC no.	4.1.2.48
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

Low-specificity L-threonine aldolase (EC 4.1.2.48, LtaE) is an enzyme with systematic name L-threonine/L-allo-threonine acetaldehyde-lyase (glycine-forming). ^{[1] [2] [3] [4] [5]} This enzyme catalyses the following chemical reactions:

L-threonine ${\displaystyle \rightleftharpoons }$ glycine + acetaldehyde

L-allothreonine ${\displaystyle \rightleftharpoons }$ glycine + acetaldehyde

This enzyme requires pyridoxal phosphate.

References

1. Yamada H, Kumagai H, Nagate T, Yoshida H (April 1970). "Crystalline threonine aldolase from Candida humicola". Biochemical and Biophysical Research Communications. 39 (1): 53–8. Bibcode:1970BBRC...39...53Y. doi:10.1016/0006-291x(70)90756-4. PMID   5438301.
2. Kumagai H, Nagate T, Yoshida H, Yamada H (March 1972). "Threonine aldolase from Candida humicola. II. Purification, crystallization and properties". Biochimica et Biophysica Acta (BBA) - Enzymology. 258 (3): 779–90. doi:10.1016/0005-2744(72)90179-9. PMID   5017702.
3. Liu JQ, Nagata S, Dairi T, Misono H, Shimizu S, Yamada H (April 1997). "The GLY1 gene of Saccharomyces cerevisiae encodes a low-specific L-threonine aldolase that catalyzes cleavage of L-allo-threonine and L-threonine to glycine—expression of the gene in Escherichia coli and purification and characterization of the enzyme". European Journal of Biochemistry. 245 (2): 289–93. doi: 10.1111/j.1432-1033.1997.00289.x . PMID   9151955.
4. Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H (July 1998). "Gene cloning, biochemical characterization and physiological role of a thermostable low-specificity L-threonine aldolase from Escherichia coli". European Journal of Biochemistry. 255 (1): 220–6. doi: 10.1046/j.1432-1327.1998.2550220.x . PMID   9692922.
5. Kim J, Kershner JP, Novikov Y, Shoemaker RK, Copley SD (November 2010). "Three serendipitous pathways in E. coli can bypass a block in pyridoxal-5'-phosphate synthesis". Molecular Systems Biology. 6: 436. doi:10.1038/msb.2010.88. PMC   3010111 . PMID   21119630.

External links

• Low-specificity+L-threonine+aldolase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)